Participation of a non-covalent phosphointermediate in ATP hydrolysis by the sarcoplasmic reticulum Ca2(+)-cotransport ATPase

With increasing SDS/protein ratios, covalent phosphorylation by ATP and Pi is abolished before ATP hydrolysis (Pi production) ceases. We have shown that the SDS-dependent profiles of the decline in covalent phosphorylation by either substrate are virtually identical, reflecting a common mechanism of...

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Bibliographic Details
Published inEuropean journal of biochemistry Vol. 192; no. 3; pp. 627 - 631
Main Authors Fassold, E, Hasselbach, W, Küchler, B
Format Journal Article
LanguageEnglish
Published England 24.09.1990
Subjects
Adenosine Triphosphate - chemistry
Adenosine Triphosphate - metabolism
Adenosine Triphosphate - pharmacology
Animals
Binding Sites
Calcium - metabolism
Calcium-Binding Proteins - physiology
Calcium-Transporting ATPases - metabolism
Hydrolysis
Lysine - chemistry
Phosphoproteins - biosynthesis
Phosphorylation
Rabbits
Sarcoplasmic Reticulum - enzymology
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Summary:With increasing SDS/protein ratios, covalent phosphorylation by ATP and Pi is abolished before ATP hydrolysis (Pi production) ceases. We have shown that the SDS-dependent profiles of the decline in covalent phosphorylation by either substrate are virtually identical, reflecting a common mechanism of detergent interaction, while ATP can be hydrolysed via a non-covalent phosphointermediate. Our studies support that the transfer of both terminal Pi from ATP, as well as Pi to its final binding site, is a multistep reaction involving electrostatic interaction with one or more amino acid side chains, including a Lys residue.
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ISSN:0014-2956